The studies proposed in this grant include establishment of amino acid and monosaccharide sequences, disulphide alignment and conformational profile particularly of human FSH and comparison with other glycoprotein hormones (LH, TSH and hCG). On the basis of above studies the effect of modifications of specific amino acid and carbohydrate residues on biological and immunological activity, subunit interaction, physicochemical properties and on conformation of the hormones will be studied. The subunits will be chemically modified to produce analogues with enhanced or antihormone activity. Peptides containing amino acid sequences of various regions of the beta-subunit (possibly in the vicinity of 'active core') will be chemically synthesized and tested for hormonal antigenic activities before and after combining with amino acid linked carbohydrate moieties by photolysis or by bifunctional reagents. Amino acid sequence of the FSH from horse, the only other species besides human will be completed. Similarly, with the availability of up to 100 or more liters of human amniotic fluid and the development of a method to isolate prolactin, the amino acid sequence of amniotic fluid prolactin is proposed. A complete physico-chemical, biological and immunological characterization of 'Big' hormones (FSH, LH, TSH, GH, PRL) will be performed to understand metabolic roles of these entities.